Structural analysis of herpes simplex virus by optical super-resolution imaging

Laine, Romain F.; Albecka, Anna; van de Linde, Sebastian; Rees, Eric J.; Crump, Colin M.; Kaminski, Clemens F.

The diameter obtained here for VP16 is in good agreement with the observation that it interacts with a number of envelopeanchored proteins 41, 42 and therefore is expected to localize close to the envelope. For VP1/2, it has been shown that the Cterminus of VP1/2 interacts with the minor capsid protein pUL25 (ref. 43 ), but the structure and the spatial arrangement of the remaining part of this large protein remains elusive. Here we were able to show that the binding site for the VP1/2-specific antibody used here (located between the amino acids 1564 and 1876) resides very close to the edge of the capsid. Furthermore, despite the common view of pUL37 as an inner tegument protein (notably because it interacts with VP1/2 (ref. 12)), the data we obtained here provide evidence that pUL37 is located at a similar position in the tegument to VP16 and, hence, closer to the outer part of the virion than previously thought.